Structure-based Drug Design on Mycobacterium tuberculosis (Mtb) targeting unsaturated-phospholipid methyltransferase - An In silico analysis.
Harsha Upadhyay and Jaishree Sikka*
Department of Botany P.M.B. Gujrati Science College Indore-452001 (India) jaiusikka@hotmail.com harshadubey2008@gmail.com
ABSTRACT
Bacteria control the biophysical properties of their membranes to allow them to thrive in a wide range of physical environments6. Mycobacterium tuberculosis (Mtb) contains an unsaturatedphospholipid methyltransferase (UPM) which is associated with the transferase family, especially those who move methyltransferase onecarbon group16. Deactivation of the UPM gene coding region is necessary to weaken the activity of Mtb bacteria; therefore, disrupting the function of the UPM was the study goal. This study helps to understand the effective inhibitors, which can inhibit the function of UPM. The protein sequence of UPM has been retrieved from the Swiss-Prot database. Structural similarity search has been performed to find templates by standalone BLAST against the PDB database. BLAST shows the protein 3D structure of the UPM, hence it has been downloaded from the PDB database and docking studies have been carried out with the same.